Merging extracellular domains: fold prediction for laminin G-like and amino-terminal thrombospondin-like modules based on homology to pentraxins.
Using a new method for construction and database searches of sequence consensus strings, we have identified a new superfamily of protein modules comprising laminin G, thrombospondin N and the pentraxin families. The conserved patterns correspond mainly to hydrophobic core residues located in central beta strands of the known three-dimensional structures of two pentraxins, the human C-reactive protein and the serum amyloid P-component. Thus, we predict a similar jellyroll fold for all members of this superfamily. In addition, the conservation of two exposed aspartate residues in the majority of superfamily members suggests hitherto unrecognised functional sites.
Beckmann
G
G
Max-Delbrück-Centre for Molecular Medicine, Robert-Rössl3-Str.10, Berlin-Buch, 13122, Germany.
Hanke
J
J
Bork
P
P
Reich
J G
JG
D000595:Amino Acid Sequence; D002097:C-Reactive Protein / Q000737:chemistry*; D006801:Humans; D007797:Laminin / Q000737:chemistry*; D008969:Molecular Sequence Data; D017510:Protein Folding; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D000683:Serum Amyloid P-Component / Q000737:chemistry*; D019699:Thrombospondins / Q000737:chemistry*; D000099153:Pentraxins
D002097:C-Reactive Protein; D007797:Laminin; D000683:Serum Amyloid P-Component; D019699:Thrombospondins; D000099153:Pentraxins